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BIO 481 Microbiology > Ch 10 Intro Metabolism > Flashcards

Ch 10 Intro Metabolism Flashcards

1
Q

Chemical work

A

Synthesis of complex bio molecules from simpler ones (anabolism)

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2
Q

Transport work

A

Take up nutrients, export waste & maintain ion balances

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3
Q

Mechanical work

A

Cell motility and movement of structures within cell.

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4
Q

Energy

A

Capacity to do work

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5
Q

ATP

A

Adenosine 5’-triphosphate a high E molecule used as cells energy currency

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6
Q

Thermodynamics

A

Study of E changes in a system

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7
Q

1st Law of Thermodynamics

A

E neither created nor destroyed

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8
Q

2nd Law of Thermodynamics

A

Chemical and physical processes proceed such that Entropy increases

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9
Q

Entropy

A

Measure of randomness and/or disorder

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10
Q

Exothermic reactions

A

Give off heat.

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11
Q

Endothermic reactions

A

Absorb heat

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12
Q

Calorie

A

Amt of heat E need to raise 1g water 1 degree C

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13
Q

Joules

A

Units of work capable of being done

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14
Q

Enthalpy

A

Heat content in a system

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15
Q

Free E change

A

Amount of E in a system available to do useful work at constant temp and pressure

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16
Q

Reactions occur spontaneously when

A

The free E of the system decreases

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17
Q

Equilibrium

A

State where no net change is occurring & free E is at a minimum (forward rxn = reverse rxn)

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18
Q

Equilibrium constant ( Keq)

A

[C][D] / [A][B]
( >1 then more products than reactants at equilibrium and will proceed as written

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19
Q

Standard free E change (delta G degree)

A

Free E change for a process at defined conditions of [], pressure, pH, and temp

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20
Q

Delta G degree apostrophe

A

Standard free E change when pH is 7 ( ie most cells)
= -2.303 RT x log Keq
(R=gas constant T=absolute temp)

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21
Q

Gas Constant (R)

A

1.9872 cal/ mol-degree
8.3145 J/mol-degree

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22
Q

Exergonic reaction

A

A rxn than spontaneously goes to completion. Standard free E change is NEGATIVE, Keq > 1

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23
Q

Energy earned

A

Exergonic reactions ( Neg delta G)

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24
Q

Energy spent

A

Endergonic reactions ( used by cells to make ATP to “store” E)

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25
Q

ADP

A

Adenosine diphosphate

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26
Q

Orthophosphate

A

Pi

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27
Q

High phosphate transfer potential

A

Phosphorylated compound will readily transfer a phosphoryl grp to another molecule (large release of energy occurs)

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28
Q

Substrate level phosphorylation

A

Making ATP using phoshoenolpyruvate (PEP) as source for phosphoryl group

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29
Q

Redox reactions

A

Reactions involving the transfer of electrons from a electron donor to an electron acceptor

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30
Q

e- donor

A

Also called reducing agent or reductant. Donates the e- to the acceptor in a redox rxn

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31
Q

e- acceptor

A

Also called oxidizing agent or oxidant. Accepts e- from the donor in a redox rxn.

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32
Q

More e- on a molecule means

A

More E for that molecule to donate

33
Q

Conjugate redox pair

A

e- acceptor and e- donor of redox half reaction

34
Q

Equilibrium constant for redox half rxn

A

Standard reduction potential (E0) ( measure of the tendency of the donor half to lose e-, measured in volts)

35
Q

Redox rxn tower trend

A

Half Rxn w/ more - E0 pair with half rxn with more + E0 (rxns further apart tend to pair well)

36
Q

NAD+

A

Nicotinamide adenine dinucleotide

37
Q

Electron transport chain (ETC)

A

Series of e- carriers that work together to transfer e- from donors to acceptors (like O2) AKA electron transport system. Embedded in a membrane.

38
Q

Molecules involved in ETC

A

NAD+, NADP+, cytochromes, heme proteins, nonheme proteins, coenzyme Q, flavin adenine dinucleotide (FAD) flavin mononucleotide (FVN)

39
Q

E0 trend in ETC

A

1st ETC most negative E0, ea slightly less so spontaneous transfer occurs

40
Q

Metabolites

A

Products of the many reactions carried out by the cell

41
Q

Biochemical pathways

A

Sets of chemical rxns preformed by organisms that convert starting substrate to one or more products

42
Q

Metabolite flux

A

Turnover rate of metabolite ( rate it is produced and then used up)

43
Q

Enzymes

A

Protein catalyst

44
Q

Catalyst

A

Substance that increases the rate of chemical rxn without being changed permanently

45
Q

How many general classes of enzymes?

A

6: Oxidireductase, Transferase, Hydrolase, Lyase, Isomerase, Ligase

46
Q

Oxidoreductase

A

Redox reactions

47
Q

Transferase

A

Rxns involving transfer of chemical groups between molecules

48
Q

Hydrolase

A

Hydrolysis

49
Q

Lyase

A

Breaking of bonds by means other than hydrolysis

50
Q

Isomerase

A

Rearrange molecules to isomer form

51
Q

Ligase

A

Joining two molecules using ATP or other nucleoside triphosphate

52
Q

Apoenzyme

A

Enzyme that requires a cofactor

53
Q

Cofactor

A

Non protein component required for catalytic activity

54
Q

Holoenzyme

A

Complete apoenzyme and cofactor complex

55
Q

Cofactor tightly (covalently) linked to apoenzyme

A

Prosthetic group

56
Q

Loosely attached, able to dissociate cofactor

57
Q

Activation energy

A

Energy required to bring substrate molecules together in correct way for reaction to occur. (reach the transition state complex)

58
Q

Active site

A

Aka catalytic site. Location on enzyme where substrate enzyme complex is formed to catalyze the rxn

59
Q

How do enzymes lower activation energy?

A

Bind substrates at the active site in the correct orientation for rxn to occur

60
Q

Michaelis constant (Km)

A

Substrate concentration required for enzyme to reach half maximal velocity (used to quantify the affinity of enzyme for substrate)

61
Q

What does lower Km mean?

A

Lower substrate concentration at which enzyme catalyzes the rxn (low Km=high affinity for substrate

62
Q

Competitive inhibitor

A

Molecule that inhibits enzyme function by directly competing with substrate by binding to the active site.

63
Q

Non competitive inhibitors

A

Inhibit enzyme function by binding to another site on enzyme that alters the shape of the enzyme, rendering it non functional.

64
Q

Ribozyme

A

Catalytic ribosomes

65
Q

How many ways are metabolic pathways regulated?

A

3 major ways; metabolic channeling, regulation of gene expression, posttranslational regultation

66
Q

Metabolic channeling

A

Localizing metabolites and enzymes in different parts of cells

67
Q

Compartmentation

A

Distribution of enzymes an metabolites among separate cell structures or organelles

68
Q

Regulation of gene expression

A

Regulates the synthesis of particular enzyme by changing rates of transcription and/or translation to control the amount of enzyme in cell (slow response)

69
Q

Posttranslational regulation

A

Direct stimulation or inhibition of enzyme activity, two main types: allosteric reg and covalent mod

70
Q

Allosteric Regulation

A

Allosteric enzymes are altered by non covalent binding of molecule (allosteric effector) at regulatory site separate from active site. Causes a change in enzyme conformation at active site that activates or inhibits enzyme

71
Q

Allosteric effector

A

Molecule that binds to allosteric enzymes regulatory site to activate or inhibit enzyme function

72
Q

Regulatory site

A

Site on allosteric enzyme separate from active site that binds a allosteric effector

73
Q

Covalent modification

A

Activation or inhibition of enzyme via covalent addition or removal of particular functional group (phosphoryl, methyl, or adenylyl)

74
Q

Covalent mod of E.coli glutamine synthetase

A

Each of 12 subunits can bind adenylic acid———> when all 12 have AMP not active. Removal of AMP allows glutamine formation———> the more removed the more active

75
Q

Allows for more sophisticated and varied stimuli response

A

Covalent modification systems

76
Q

Pacemaker enzyme

A

An enzyme that catalyzes the slowest (or rate determining) Rxn in a metabolic pathway

77
Q

Feedback inhibition

A

Neg feedback mech where end product inhibits the activity of an enzyme in the pathway leading to its formation. Aka end product inhibition

78
Q

Isoenzymes

A

Different forms of an enzyme that catalyze the same Rxn. Aka isozymes.

BIO 481 Microbiology (12 decks)

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